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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6735
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pubmed:dateCreated |
1999-6-24
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pubmed:databankReference |
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pubmed:abstractText |
Histone acetylation is important in chromatin remodelling and gene activation. Nearly all known histone-acetyltransferase (HAT)-associated transcriptional co-activators contain bromodomains, which are approximately 110-amino-acid modules found in many chromatin-associated proteins. Despite the wide occurrence of these bromodomains, their three-dimensional structure and binding partners remain unknown. Here we report the solution structure of the bromodomain of the HAT co-activator P/CAF (p300/CBP-associated factor). The structure reveals an unusual left-handed up-and-down four-helix bundle. In addition, we show by a combination of structural and site-directed mutagenesis studies that bromodomains can interact specifically with acetylated lysine, making them the first known protein modules to do so. The nature of the recognition of acetyl-lysine by the P/CAF bromodomain is similar to that of acetyl-CoA by histone acetyltransferase. Thus, the bromodomain is functionally linked to the HAT activity of co-activators in the regulation of gene transcription.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Bromine Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/p300-CBP Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/p300-CBP-associated factor
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
399
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
491-6
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10365964-Acetyltransferases,
pubmed-meshheading:10365964-Amino Acid Sequence,
pubmed-meshheading:10365964-Bromine Compounds,
pubmed-meshheading:10365964-Cell Cycle Proteins,
pubmed-meshheading:10365964-Crystallography, X-Ray,
pubmed-meshheading:10365964-Escherichia coli,
pubmed-meshheading:10365964-Histone Acetyltransferases,
pubmed-meshheading:10365964-Ligands,
pubmed-meshheading:10365964-Lysine,
pubmed-meshheading:10365964-Models, Molecular,
pubmed-meshheading:10365964-Molecular Sequence Data,
pubmed-meshheading:10365964-Mutagenesis, Site-Directed,
pubmed-meshheading:10365964-Protein Binding,
pubmed-meshheading:10365964-Protein Conformation,
pubmed-meshheading:10365964-Recombinant Proteins,
pubmed-meshheading:10365964-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10365964-Sequence Homology, Amino Acid,
pubmed-meshheading:10365964-Transcription Factors,
pubmed-meshheading:10365964-p300-CBP Transcription Factors
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pubmed:year |
1999
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pubmed:articleTitle |
Structure and ligand of a histone acetyltransferase bromodomain.
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pubmed:affiliation |
Structural Biology Program, Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York, New York 10029-6574, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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